The plasma-membrane ATPase of is a proton pump whose activity, essential for proliferation, is subject to regulation by nutritional signals. The previous finding that the gene product is required for the glucose-induced H-ATPase activation suggested that H-ATPase activity is regulated by cAMP. Analysis of starvation-induced inactivation and glucose-induced activation of the H-ATPase in mutants affected in activity of the proteins, adenylyl cyclase or cAMP-dependent protein kinase showed that nutritional regulation of H-ATPase activity does not depend directly on any of these factors. We conclude that adenylyl cyclase does not mediate all nutritional responses. This also indicates that the specific requirement for the glucose-induced activation of the H-ATPase identifies a new function for the gene product, a function that appears to be independent of -mediated modulation of the /adenylyl cyclase/cAMP pathway.


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